To approach to the goal of predicting the three-dimensional structure on the basis of the amino acid sequence translated from the genetic information, we investigate the global cooperative interactions which evolve only in the late phase of folding to stabilize the structure. The kinetic and thermodynamic studies of folding of the fragment complexes from horse cytochrome c and the kinetic studies of folding of the fragment complexes from tuna cytochrome c have indicated that 1) the native or native-like complexes can assume different energy states 2) the transition between these energy states may occur by modulation of the global cooperative interactions without a large change in conformation (no large change in the environment of non-polar groups) 3) this transition is thermodynamically characterized by a large change in entropy and enthalpy (entropy-enthalpy compensation) 4) the reduction-oxidation potential of cytochrome c may also be modulated by change of global cooperative interactions. Similar conclusions have also been reached by studies of the conformational dynamics of biologically active three-fragment complex of cytochrome c.